Among the topics in DAT research that can be readily studied in nonneural cells (including tissue cultures) are molecular genetics, amyloid precursor protein formation and metabolism, systemic manifestations of immunological and inflammatory mechanisms, proteolysis, membranes, signal transduction, and mitochondria and metabolism.
Perisomatic sprouts immunoreactive for nerve growth factor receptor and neurofibrillary degeneration affect different neuronal populations in the basal nucleus in patients with Alzheimer's disease.
Abnormal phosphorylation of the microtubule associated protein tau component of neurofibrillary tangles (NFTs) in Alzheimer's disease (AD) may result from alterations in protein kinase expression.
Neuropathological findings in cerebral B-protein amyloidosis. Differences and similarities in those cases presenting as a cerebral hemorrhage and those presenting as a dementia of the Alzheimer type.
This finding of AD-specific and age-related change led us to the idea that a relative increase in KPI-harboring APPs over a KPI-lacking APP may perturb normal degradation of APPs, thereby leading to deposition of beta A4 protein as amyloid.
Because phosphorylation of EF-2 inhibits protein synthesis, the observed AD-associated phosphorylation of EF-2 is consistent with the reduced in vitro activity of polysomes isolated from AD tissues that we have previously reported.
A recent report by Petruzzella et al.(BBRC 186, 491-497, 1992) raised a question as to whether a point mutation in the mitochondrial ND2 gene (BBRC 182, 238-246, 1992) is relevant to Alzheimer's disease.
The Indiana kindred variant of Gerstmann-Sträussler-Scheinker disease has amyloid plaques that contain prion protein (PrP), but is atypical because neurofibrillary tangles like those of Alzheimer disease are present.
The study of the mechanism by which the amyloid beta-peptide arises from the amyloid precursor protein is very important in order to understand the biological basis of amyloid deposition and its role in Alzheimer's disease.
The development of models of AD using the APP mutations offers the possibility of identifying drug targets and developing more effective treatments than are presently available.
Two synthetic peptides with sequences identical with those of fragments of the extracellular domain of the Alzheimer's-diseaseamyloid precursor protein (APP) were used to raise antibodies.